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Background: The Immunoglobulin Heavy Chain (IGH) genomic region is responsible for the production of circulating antibodies and warrants careful investigation for its association with COVID-19 characteristics. Multiple allelic variants within and across different IGH gene segments form a limited set of haplotypes. Previous studies have shown associations between some of these haplotypes and clinical outcomes of COVID-19.

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Since the outbreak of the novel coronavirus (SARS-CoV-2), the world has suffered significant losses. At present, the pneumonia disease caused by SARS-CoV-2 virus has not been eliminated, and SARS-CoV-2 has a high mutation rate, and its variant strains also have a high prevalence rate, which has always threatened the health of all mankind. This study aims to develop a rapid and sensitive method to complement existing SARS-CoV-2 diagnostic tools by utilizing surface-enhanced Raman spectroscopy (SERS) for the direct detection of the intrinsic SERS signal from the S proteins of SARS-CoV-2 and its variants (Omicron and Delta) within 5 min using a portable Raman spectrometer.

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Structure of a zoonotic H5N1 hemagglutinin reveals a receptor-binding site occupied by an auto-glycan.

Structure

January 2025

Aaron Diamond AIDS Research Center, Columbia University Vagelos College of Physicians and Surgeons, New York, NY 10032, USA; Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10027, USA. Electronic address:

Highly pathogenic avian influenza has spilled into many mammals, most notably cows and poultry, with several dozen human breakthrough infections. Zoonotic crossovers, with hemagglutinins mutated to enhance viral ability to use human α2-6-linked sialic acid receptors versus avian α2-3-linked ones, highlight the pandemic risk. To gain insight into these crossovers, we determined the cryoelectron microscopy (cryo-EM) structure of the hemagglutinin from the zoonotic H5N1 A/Texas/37/2024 strain (clade 2.

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Transmission of Zika virus (ZIKV) has been reported in 92 countries and the geographical spread of invasive virus-borne vectors has increased in recent years. Arboviruses naturally survive between vertebrate hosts and arthropod vectors. Transmission success requires the mosquito to feed on viraemic hosts.

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Human cytomegalovirus (HCMV) encodes four viral Fc-gamma receptors (vFcγRs) that counteract antibody-mediated activation in vitro, but their role in infection and pathogenesis is unknown. To examine their in vivo function in an animal model evolutionarily closely related to humans, we identified and characterized Rh05, Rh152/151 and Rh173 as the complete set of vFcγRs encoded by rhesus CMV (RhCMV). Each one of these proteins displays functional similarities to their prospective HCMV orthologs with respect to antagonizing host FcγR activation in vitro.

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